ID G5EDT4_CAEEL Unreviewed; 927 AA.
AC G5EDT4;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=IgGFc-binding protein-like {ECO:0000313|EMBL:CAB03262.1};
GN ORFNames=CELE_T01D3.6 {ECO:0000313|EMBL:CAB03262.1}, T01D3.6
GN {ECO:0000313|EMBL:CAB03262.1, ECO:0000313|WormBase:T01D3.6a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAB03262.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAB03262.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAB03262.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; BX284605; CAB03262.1; -; Genomic_DNA.
DR RefSeq; NP_506394.1; NM_073993.3.
DR AlphaFoldDB; G5EDT4; -.
DR SMR; G5EDT4; -.
DR STRING; 6239.T01D3.6a.1; -.
DR EPD; G5EDT4; -.
DR PaxDb; 6239-T01D3-6a; -.
DR PeptideAtlas; G5EDT4; -.
DR EnsemblMetazoa; T01D3.6a.1; T01D3.6a.1; WBGene00011330.
DR GeneID; 179863; -.
DR KEGG; cel:CELE_T01D3.6; -.
DR AGR; WB:WBGene00011330; -.
DR WormBase; T01D3.6a; CE12964; WBGene00011330; -.
DR eggNOG; KOG1216; Eukaryota.
DR eggNOG; KOG2579; Eukaryota.
DR InParanoid; G5EDT4; -.
DR OMA; FRCASNG; -.
DR OrthoDB; 2872912at2759; -.
DR PhylomeDB; G5EDT4; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00011330; Expressed in larva and 3 other cell types or tissues.
DR ExpressionAtlas; G5EDT4; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd19941; TIL; 1.
DR Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR001846; VWF_type-D.
DR NCBIfam; NF040941; GGGWT_bact; 1.
DR PANTHER; PTHR46160; ALPHA-TECTORIN-RELATED; 1.
DR PANTHER; PTHR46160:SF5; PROTEIN CBG11501; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF01826; TIL; 1.
DR Pfam; PF00094; VWD; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00186; FBG; 1.
DR SMART; SM00216; VWD; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR SUPFAM; SSF57567; Serine protease inhibitors; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS51233; VWFD; 1.
PE 1: Evidence at protein level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Proteomics identification {ECO:0007829|EPD:G5EDT4,
KW ECO:0007829|PeptideAtlas:G5EDT4};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..927
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003476064"
FT DOMAIN 186..377
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 627..664
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 663..919
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DISULFID 654..663
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 927 AA; 103414 MW; 71AEF0A61FC2B266 CRC64;
MALFKHLALC LLLTLAAAED DLKCYGADCE VPHYMDDTEQ CSGLECESKE TLLAMISHYQ
KEKHDEYLAP LTKPIRDESA VRNFLNEVAV TGDLAATVSP QCSICSQPGL CNSGQCVPDA
RFPWQYFYCV CPDYASGRFC QNEIKCKDNS CGKNADCYVA NHQLNCICKP GYTARRNGRD
CDMKVQQACM SGDPHYVTYD GLRFDYQGTC PYVFSQPCTT LPAPYLWYSV RAKNELPGKG
YHISQVSEVE VDLHNLTIHV DGRSKTALVN GVQVLTPWYF PNKNTWTVRV RFSGSTFTIE
NDQGVVVTFT TYNSLCVQVP DIPEFNGATT LCGLAGNIDG KKLDDVVNKN GSVLAIKSSR
QPENNNHADF MKTEDTWITD KFLILRPGQE NCINGQTLDN NTNCVSTSIS LAQSCADVAT
ASQTCYPIQQ AEMGLGTFGA CQGLGNDTLE DFYYNCIYDI CRNPAFKCTE FTYFLQYCQL
ALPQVAMNQN WRAQINCPLA CPLNAHPSTC TSSCPSTCAE PFPEYCDQGC VDGCECDPGY
VIDNTVTGSI KCIRLDQCGC VDSDGNAHRP GKPWVTQNCT IYHECQNGTM WSDYRPCSDD
GSCVLNSIDM QCKCNNGYRG DGYNCTDINE CVETPGICGH GQCVNTPGSY HCTCDDFWLG
DNCNTYKPRR HCADLYVYWG VRESGVNSIN PPFVLPQRAK FAPMNVYCDM TTNGGGYTLM
SSDTADLNTN KTFQDYLIGF GNPATQSVWL GLEFIHQLTT YQPQNLRLNL FRCASNGRPS
LTTDCTYPTF SVLDSTTQYS VVIREACTGS EADEHYYQDG WARWDLTQNG PKFSTWDIEA
QTTIPPTLRA KMEGDAIYYT CSKSNFNTGW WYVEDQLCGA ANLNGVRYTC PVIPVENERY
LRWAEGTLGQ SWMYLRPVGF PKYDTNM
//
